Protein binding of aspirin and salicylate measured by in vivo ultrafiltration

Clinical Pharmacology and Therapeutics
P GhahramaniL E Ramsay

Abstract

Methods for measuring protein binding of drugs generally require direct measurement of the concentration of unbound drug and thus may require a highly sensitive assay. In vivo ultrafiltration has been used to determine protein binding of endogenous substances. We have examined its value for measuring protein binding of drugs because it requires measurement of only the concentration of total drug, not unbound drug, in plasma. The protein binding of aspirin and its metabolite salicylate was measured in 29 healthy subjects 20 minutes after a single oral dose of 600 mg soluble aspirin, by the new method, in vivo ultrafiltration, as well as by a standard method, in vitro ultracentrifugation. The data for salicylate were examined systematically to determine the optimal method of determining estimates of protein binding by in vivo ultrafiltration. Estimates of protein binding of salicylate were 81.7% +/- 10.1% (mean +/- SD) by the in vivo method and 81.6% +/- 11.3% by in vitro ultracentrifugation. Bland-Altman analysis of agreement showed that within-individual differences in percentage of protein binding determined by the two methods did not differ significantly from zero (mean difference, 0.07%; 95% confidence interval, -2.33 to +2....Continue Reading

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Citations

Jul 2, 2011·Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan·Takehiro YaguchiYasuhiko Yamada
May 4, 2016·Molecular Pharmaceutics·J Al-GousousP Langguth
Apr 28, 2005·European Journal of Pharmaceutical Sciences : Official Journal of the European Federation for Pharmaceutical Sciences·Nele Plock, Charlotte Kloft
Apr 24, 2017·JACC. Basic to Translational Science·George O AngheloiuCarl Whatling
Oct 28, 2008·Biochimica Et Biophysica Acta·Domenico LapennaFranco Cuccurullo
Jul 17, 1999·Analytical Chemistry·C K LariveS Bogdanowich-Knipp

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